Literature summary for 5.4.2.11 extracted from

Bond, C.S.; White, M.F.; Hunter, W.N.
Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex (2002), J. Mol. Biol., 316, 1071-1081.

Search for more literature for 5.4.2.11

Activating Compound

Activating Compound	Comment	Organism	Structure
2,3-bisphosphoglycerate	-	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of phosphohistidine activated dPGM are grown from hanging drops from a protein solution containing 15 mg/ml dPGM in 20 mM Tris-HCl, pH 8.0, with 100 mM NaCl and a reservoir comprising 100 mM Tris-HCl, pH 8.75, 200 mM Li2SO4 and 20% polyethylene glycol 4000, crystals diffrakt to 1.25 A resolution	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2-Phosphoglycerate	Escherichia coli	-	3-Phosphoglycerate	-	r

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant dPGM	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-Phosphoglycerate	-	Escherichia coli	3-Phosphoglycerate	-	r

Subunits

Subunits	Comment	Organism
dimer	crystal structure	Escherichia coli

Synonyms

Synonyms	Comment	Organism
cofactor-dependent phosphoglycerate mutase	-	Escherichia coli
DPGM	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)